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2IXH

RmlC P aeruginosa with dTDP-rhamnose

Functional Information from GO Data
ChainGOidnamespacecontents
A0005829cellular_componentcytosol
A0008830molecular_functiondTDP-4-dehydrorhamnose 3,5-epimerase activity
A0009103biological_processlipopolysaccharide biosynthetic process
A0009244biological_processlipopolysaccharide core region biosynthetic process
A0016853molecular_functionisomerase activity
A0019305biological_processdTDP-rhamnose biosynthetic process
A0045226biological_processextracellular polysaccharide biosynthetic process
B0005829cellular_componentcytosol
B0008830molecular_functiondTDP-4-dehydrorhamnose 3,5-epimerase activity
B0009103biological_processlipopolysaccharide biosynthetic process
B0009244biological_processlipopolysaccharide core region biosynthetic process
B0016853molecular_functionisomerase activity
B0019305biological_processdTDP-rhamnose biosynthetic process
B0045226biological_processextracellular polysaccharide biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues22
DetailsBINDING SITE FOR RESIDUE TRH A1185
ChainResidue
APHE22
ATYR134
ATRP140
ALYS170
AHOH2229
AHOH2253
AHOH2281
AHOH2282
AHOH2283
AHOH2284
AHOH2285
AARG26
AHOH2286
AHOH2287
AHOH2288
APHE29
AGLU31
AGLN50
AARG62
AHIS65
ALYS74
AHIS121

site_idAC2
Number of Residues22
DetailsBINDING SITE FOR RESIDUE TRH B1185
ChainResidue
BPHE22
BARG26
BPHE29
BGLU31
BGLN50
BARG62
BHIS65
BLYS74
BHIS121
BTYR134
BTRP140
BLYS170
BHOH2272
BHOH2293
BHOH2294
BHOH2295
BHOH2296
BHOH2297
BHOH2298
BHOH2299
BHOH2300
BHOH2301

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:17046787
ChainResidueDetails
AHIS65
BHIS65

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:17046787
ChainResidueDetails
ATYR134
BTYR134

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:17046787, ECO:0007744|PDB:2IXI, ECO:0007744|PDB:2IXK
ChainResidueDetails
AARG26
AGLU31
BARG26
BGLU31

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:17046787, ECO:0007744|PDB:2IXH
ChainResidueDetails
AGLN50
BGLN50

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:17046787, ECO:0000269|Ref.3, ECO:0007744|PDB:1RTV, ECO:0007744|PDB:2IXH, ECO:0007744|PDB:2IXJ, ECO:0007744|PDB:2IXK
ChainResidueDetails
AARG62
BARG62

site_idSWS_FT_FI6
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:17046787, ECO:0000269|Ref.3, ECO:0007744|PDB:1RTV, ECO:0007744|PDB:2IXH, ECO:0007744|PDB:2IXI, ECO:0007744|PDB:2IXJ, ECO:0007744|PDB:2IXK
ChainResidueDetails
ALYS74
AHIS121
BLYS74
BHIS121

site_idSWS_FT_FI7
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:17046787, ECO:0000269|Ref.3, ECO:0007744|PDB:1RTV, ECO:0007744|PDB:2IXJ
ChainResidueDetails
AGLU145
BGLU145

site_idSWS_FT_FI8
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:17046787, ECO:0007744|PDB:2IXH, ECO:0007744|PDB:2IXK
ChainResidueDetails
ALYS170
BLYS170

site_idSWS_FT_FI9
Number of Residues2
DetailsSITE: Participates in a stacking interaction with the thymidine ring of dTDP-4-oxo-6-deoxyglucose => ECO:0000250|UniProtKB:Q5SFD1
ChainResidueDetails
ATRP140
BTRP140

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 329
ChainResidueDetails
AHIS65proton acceptor, proton donor
ALYS74electrostatic stabiliser
ATYR134proton acceptor, proton donor, proton relay
AASP171electrostatic stabiliser, increase acidity, increase basicity

site_idMCSA2
Number of Residues4
DetailsM-CSA 329
ChainResidueDetails
BHIS65proton acceptor, proton donor
BLYS74electrostatic stabiliser
BTYR134proton acceptor, proton donor, proton relay
BASP171electrostatic stabiliser, increase acidity, increase basicity

218853

PDB entries from 2024-04-24

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